Journal
ANNUAL REVIEW OF BIOPHYSICS
Volume 37, Issue -, Pages 135-151Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.biophys.36.040306.132812
Keywords
free energy; enthalpy; entropy; binding; rational drug design
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Funding
- NCI NIH HHS [CA35635] Funding Source: Medline
- NIGMS NIH HHS [GM077422] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R01CA035635] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM077422] Funding Source: NIH RePORTER
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Modern instrumentation for calorimetry permits direct determination of enthalpy values for binding reactions and conformational transitions in biomolecules. Complete thermodynamic profiles consisting of free energy, enthalpy, and entropy may be obtained for reactions of interest in a relatively straightforward manner. Such profiles are of enormous value in drug design because they provide information about the balance of driving forces that cannot be obtained from structural or computational methods alone. This perspective shows several examples of the insight provided by thermodynamic data in drug design.
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